The 5' noncoding region (NCR) of poliovirus RNA is folded into a compl
ex structure comprised of multiple, critically spaced, stem-loop domai
ns. Mutations in at least one of these domains markedly affects the ne
urovirulence of the virus. Two proteins have been identified recently
which bind and apparently mediate functions of the 5' NCR in translati
on. We have demonstrated specific binding of three additional proteins
in a Hela cell ribosomal salt wash that can be crosslinked to specifi
c stem-loop segments of the 5' NCR. These same RNA segments inhibit tr
anslation of polio RNA in vitro, presumably by competing for protein b
inding. The Sabin vaccine strain of polio RNA exhibits a reduced affin
ity of binding for specific proteins. The determinant for this reducti
on appears to be a single nucleotide difference at position 480 betwee
n the neurovirulent and attenuated viral strains.